FUT3_PANTR
ID FUT3_PANTR Reviewed; 372 AA.
AC O19058;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3 {ECO:0000250|UniProtKB:P21217};
DE EC=2.4.1.65 {ECO:0000250|UniProtKB:P21217};
DE AltName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase;
DE EC=2.4.1.152 {ECO:0000250|UniProtKB:P21217};
DE AltName: Full=Alpha-3-fucosyltransferase FUT3 {ECO:0000250|UniProtKB:P21217};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:P21217};
DE AltName: Full=Alpha-3/4-fucosyltransferase {ECO:0000250|UniProtKB:Q8HYJ5};
DE AltName: Full=Blood group Lewis alpha-4-fucosyltransferase;
DE Short=Lewis FT;
DE AltName: Full=Fucosyltransferase 3;
DE AltName: Full=Fucosyltransferase III;
DE Short=FucT-III;
GN Name=FUT3 {ECO:0000250|UniProtKB:P21217};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-162 AND MET-304.
RX PubMed=9368041; DOI=10.1074/jbc.272.47.29721;
RA Costache M., Apoil P.-A., Cailleau A., Elmgren A., Larson G., Henry S.,
RA Blancher A., Iordachescu D., Oriol R., Mollicone R.;
RT "Evolution of fucosyltransferase genes in vertebrates.";
RL J. Biol. Chem. 272:29721-29728(1997).
CC -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine
CC (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids
CC and oligosaccharides via an alpha(1,4) linkage, and the subterminal
CC glucose (Glc) or GlcNAc of type 2 chain (beta-D-Gal-(1->4)-beta-D-
CC GlcNAc) oligosaccharides via an alpha(1,3) linkage, independently of
CC the presence of terminal alpha-L-fucosyl-(1,2) moieties on the terminal
CC galactose of these acceptors and participates in the blood groups Lewis
CC determination and expression of Lewis a (Le(a)), lewis b (Le(b)), Lewis
CC x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens. Also catalyzes the
CC transfer of L-fucose to subterminal GlcNAc of sialyl- and disialyl-
CC lactotetraosylceramide to produce sialyl Lewis a (sLe(a)) and disialyl
CC Lewis a via an alpha(1,4) linkage and therefore may regulate cell
CC surface sialyl Lewis a expression and consequently regulates adhesive
CC properties to E-selectin, cell proliferation and migration. Catalyzes
CC the transfer of an L-fucose to 3'-sialyl-N-acetyllactosamine by an
CC alpha(1,3) linkage, which allows the formation of sialyl-Lewis x
CC structure and therefore may regulate the sialyl-Lewis x surface antigen
CC expression and consequently adhesive properties to E-selectin. Prefers
CC type 1 chain over type 2 acceptors. Type 1 tetrasaccharide is a better
CC acceptor than type 1 disaccharide suggesting that a beta anomeric
CC configuration of GlcNAc in the substrate is preferred. Lewis-positive
CC (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-))
CC individuals have an inactive enzyme. {ECO:0000250|UniProtKB:P21217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-
CC fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC Xref=Rhea:RHEA:23628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:140304;
CC EC=2.4.1.65; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23629;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-
CC N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an
CC alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-
CC GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:136545, ChEBI:CHEBI:139509;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:137941;
CC EC=2.4.1.152; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative +
CC GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-
CC L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-
CC (1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:52864,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145342, ChEBI:CHEBI:145343;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + Lc4Cer = a lactoside III(4)-a-Fuc-Lc4Cer +
CC GDP + H(+); Xref=Rhea:RHEA:48824, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90800,
CC ChEBI:CHEBI:90811; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48825;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = GDP + H(+) +
CC III(4)-a-Fuc-Lc4Cer(d18:1(4E)); Xref=Rhea:RHEA:48328,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90292;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48329;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->3)-[N-acetyl-alpha-neuraminosyl-(2->6)]-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-N-acyl-sphing-4-enine = GDP + H(+) + N-acetyl-alpha-
CC neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-alpha-L-fucosyl-(1->4)-
CC [N-acetyl-alpha-neuraminosyl-(2->6)-N-acetyl-beta-D-glucosaminyl-
CC (1->3)]-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-
CC sphing-4-enine; Xref=Rhea:RHEA:47892, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88079,
CC ChEBI:CHEBI:88089; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47893;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine =
CC GDP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC (1->3)-alpha-L-fucosyl-(1->4)-[N-acetyl-beta-D-glucosaminyl-(1->3)]-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-
CC enine; Xref=Rhea:RHEA:47888, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:88073, ChEBI:CHEBI:88088;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47889;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + GDP-beta-L-
CC fucose = beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-
CC D-glucosamine + GDP + H(+); Xref=Rhea:RHEA:62844, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27707, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:62265; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62845;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-D-GlcNAc + GDP-beta-L-
CC fucose = alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-
CC GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62896, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:59440,
CC ChEBI:CHEBI:62259; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62897;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc + GDP-beta-L-
CC fucose = alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-
CC GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62900, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:62263,
CC ChEBI:CHEBI:62507; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62901;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + GDP-beta-L-
CC fucose = beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-
CC D-glucosamine + GDP + H(+); Xref=Rhea:RHEA:62824, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:60152,
CC ChEBI:CHEBI:62287; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62825;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + lactose = beta-D-galactosyl-(1->4)-[alpha-
CC L-fucosyl-(1->3)]-D-glucose + GDP + H(+); Xref=Rhea:RHEA:62888,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17716, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90065;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62889;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative +
CC GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-
CC L-Fuc-(1->4)]-beta-D-GlcNAc derivative + GDP + H(+);
CC Xref=Rhea:RHEA:62904, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:146021, ChEBI:CHEBI:146022;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62905;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P21217}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P21217}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P21217}. Note=Membrane-bound form in trans
CC cisternae of Golgi. {ECO:0000250|UniProtKB:P21217}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P21217}.
CC -!- POLYMORPHISM: There are two alleles, A and B. Allele A has Arg-162 and
CC Val-304. Allele B has Gly-162 and Met-304.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; Y14033; CAA74360.1; -; Genomic_DNA.
DR RefSeq; NP_001009149.1; NM_001009149.1.
DR AlphaFoldDB; O19058; -.
DR STRING; 9598.ENSPTRP00000054902; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR PaxDb; O19058; -.
DR GeneID; 493975; -.
DR KEGG; ptr:493975; -.
DR CTD; 2525; -.
DR eggNOG; KOG2619; Eukaryota.
DR InParanoid; O19058; -.
DR BRENDA; 2.4.1.65; 4497.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017060; F:3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0017083; F:4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0036065; P:fucosylation; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISS:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR031481; Glyco_tran_10_N.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF17039; Glyco_tran_10_N; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..372
FT /note="3-galactosyl-N-acetylglucosaminide 4-alpha-L-
FT fucosyltransferase FUT3"
FT /id="PRO_0000221097"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000250|UniProtKB:P21217, ECO:0000255"
FT TOPO_DOM 35..372
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 40..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 162
FT /note="R -> G (in allele B)"
FT /evidence="ECO:0000269|PubMed:9368041"
FT /id="VAR_018692"
FT VARIANT 304
FT /note="V -> M (in allele B)"
FT /evidence="ECO:0000269|PubMed:9368041"
FT /id="VAR_018693"
SQ SEQUENCE 372 AA; 43234 MW; 649CBF8BCA7BD74C CRC64;
MDPLGAAKPQ WPWRRCLAAL LFQLLVAVCF FSYLRVSRDD ATGSPRPGLM AVEPVTGAPS
GSSRQDTTPT RPTLLILLWT WPFHIPVALS RCSEMVPGAA DCHITADRKV YPQADAVIVH
HWDIMYNPKS RLPPSPRPQG QRWIWFNLEP PPNCQHLEAL DRYFNLTMSY RSDSDIFTPY
GWLEPWSGQP AHPPLNLSAK TELVAWAVSN WKLDSARVRY YQSLQAHLKV DVYGRSHKPL
PKGTMMETLS RYKFYLAFEN SLHPDYITEK LWRNALEAWA VPVVLGPSRS NYERFLPPDA
FIHVDDFQSP KDLARYLQEL DKDHARYLSY FRWRETLRPR SFSWALDFCK ACWKLQQESR
YQTMRSIAAW FT
